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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Hiscox, Julian A. Trinh, Chi H. Carroll, Miles W. Barr, John N. Tanner, Sian J. Richard, Charles-adrien Dods, Rachel L. Edwards, Thomas A. Eléouët, Jean-françois Ariza, Antonio Wu, Weining Blondot, Marie-lise Kyle, Hannah F. Trincão, José Silman, Nigel J. |
| Description | Author Affiliation: Tanner SJ ( Astbury Centre for Structural Molecular Biology and School of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom.); |
| Abstract | The M2-1 protein of the important pathogen human respiratory syncytial virus is a zinc-binding transcription antiterminator that is essential for viral gene expression. We present the crystal structure of full-length M2-1 protein in its native tetrameric form at a resolution of 2.5 Å. The structure reveals that M2-1 forms a disk-like assembly with tetramerization driven by a long helix forming a four-helix bundle at its center, further stabilized by contact between the zinc-binding domain and adjacent protomers. The tetramerization helix is linked to a core domain responsible for RNA binding activity by a flexible region on which lie two functionally critical serine residues that are phosphorylated during infection. The crystal structure of a phosphomimetic M2-1 variant revealed altered charge density surrounding this flexible region although its position was unaffected. Structure-guided mutagenesis identified residues that contributed to RNA binding and antitermination activity, revealing a strong correlation between these two activities, and further defining the role of phosphorylation in M2-1 antitermination activity. The data we present here identify surfaces critical for M2-1 function that may be targeted by antiviral compounds. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 4 |
| Volume Number | 111 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2014-01-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Respiratory Syncytial Viruses Metabolism Viral Proteins Chemistry Biopolymers Crystallography, X-Ray Nuclear Magnetic Resonance, Biomolecular Phosphorylation Protein Conformation RNA Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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